Gpi16 is the PIG-T-family accessory subunit of the endoplasmic-reticulum GPI-anchor transamidase complex. Its large lumenal domain and C-terminal membrane anchor support assembly and function of the machinery that attaches preformed GPI anchors to proteins. The catalytic cleavage/transamidation chemistry belongs to the Gpi8/PIG-K subunit, rather than to Gpi16 alone.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003674 molecular_function | ND GO_REF:0000015 | ACCEPT | Summary: An autonomous molecular activity has not been established for Gpi16. Reason: Retain the ND root annotation: accessory complex membership and participation in GPI attachment do not establish an independently enabled transamidase activity. Supporting Evidence: file:SCHPO/gpi16/gpi16-uniprot.txt CC -!- FUNCTION: Component of the GPI transamidase complex. Involved in CC transfer of GPI to proteins (By similarity). {ECO:0000250}. |
| GO:0005783 endoplasmic reticulum | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | MODIFY | Summary: Gpi16 is an ER membrane protein. Reason: The target localization atlas and type-I membrane topology resolve the broader ER location to its membrane. Proposed replacements: endoplasmic reticulum membrane Supporting Evidence: file:SCHPO/gpi16/gpi16-uniprot.txt CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: Gpi16 resides in the ER membrane. Reason: The target localization record and PIG-T topology support this compartment. The ComplexPortal NAS attribution is curated complex inference, not a direct Gpi16 localization experiment in the cited prediction-method paper. Supporting Evidence: file:SCHPO/gpi16/gpi16-uniprot.txt CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | NAS PMID:15003443 A sensitive predictor for potential GPI lipid modification s... | ACCEPT | Summary: Gpi16 resides in the ER membrane. Reason: The target localization record and PIG-T topology support this compartment. The ComplexPortal NAS attribution is curated complex inference, not a direct Gpi16 localization experiment in the cited prediction-method paper. Supporting Evidence: file:SCHPO/gpi16/gpi16-uniprot.txt CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0006506 GPI anchor biosynthetic process | IEA GO_REF:0000041 | MODIFY | Summary: Gpi16 participates in attachment of a preassembled GPI anchor to proteins. Reason: The transamidase acts at the protein-attachment step rather than specifying lipid-anchor precursor synthesis. Proposed replacements: attachment of GPI anchor to protein Supporting Evidence: file:SCHPO/gpi16/gpi16-uniprot.txt CC -!- FUNCTION: Component of the GPI transamidase complex. Involved in CC transfer of GPI to proteins (By similarity). {ECO:0000250}. |
| GO:0016255 attachment of GPI anchor to protein | IBA GO_REF:0000033 | ACCEPT | Summary: Gpi16 contributes to GPI-anchor attachment as a transamidase-complex subunit. Reason: PIG-T family identity and curated complex composition support this biological process through orthology. No autonomous catalytic activity is inferred; the NAS paper is indirect context rather than a target assay. Supporting Evidence: file:SCHPO/gpi16/gpi16-uniprot.txt CC -!- FUNCTION: Component of the GPI transamidase complex. Involved in CC transfer of GPI to proteins (By similarity). {ECO:0000250}. PMID:11598210 These complexes can be affinity purified and are shown to consist of Gaa1p, Gpi8p, and Gpi16p (YHR188c). PMID:11483512 PIG-T maintains the complex by stabilizing the expression of GAA1 and GPI8. |
| GO:0016255 attachment of GPI anchor to protein | IEA GO_REF:0000002 | ACCEPT | Summary: Gpi16 contributes to GPI-anchor attachment as a transamidase-complex subunit. Reason: PIG-T family identity and curated complex composition support this biological process through orthology. No autonomous catalytic activity is inferred; the NAS paper is indirect context rather than a target assay. Supporting Evidence: file:SCHPO/gpi16/gpi16-uniprot.txt CC -!- FUNCTION: Component of the GPI transamidase complex. Involved in CC transfer of GPI to proteins (By similarity). {ECO:0000250}. PMID:11598210 These complexes can be affinity purified and are shown to consist of Gaa1p, Gpi8p, and Gpi16p (YHR188c). PMID:11483512 PIG-T maintains the complex by stabilizing the expression of GAA1 and GPI8. |
| GO:0016255 attachment of GPI anchor to protein | NAS PMID:15003443 A sensitive predictor for potential GPI lipid modification s... | ACCEPT | Summary: Gpi16 contributes to GPI-anchor attachment as a transamidase-complex subunit. Reason: PIG-T family identity and curated complex composition support this biological process through orthology. No autonomous catalytic activity is inferred; the NAS paper is indirect context rather than a target assay. Supporting Evidence: file:SCHPO/gpi16/gpi16-uniprot.txt CC -!- FUNCTION: Component of the GPI transamidase complex. Involved in CC transfer of GPI to proteins (By similarity). {ECO:0000250}. PMID:11598210 These complexes can be affinity purified and are shown to consist of Gaa1p, Gpi8p, and Gpi16p (YHR188c). PMID:11483512 PIG-T maintains the complex by stabilizing the expression of GAA1 and GPI8. |
| GO:0031505 fungal-type cell wall organization | NAS PMID:15003443 A sensitive predictor for potential GPI lipid modification s... | KEEP AS NON CORE | Summary: GPI attachment supports fungal cell-wall protein deployment. Reason: This is a downstream consequence of maturation of GPI-anchored proteins; the molecular role of Gpi16 is in the ER transamidase complex. Retain the curated ComplexPortal context without treating cell-wall organization as an independent biochemical activity. Supporting Evidence: file:SCHPO/gpi16/gpi16-uniprot.txt CC -!- FUNCTION: Component of the GPI transamidase complex. Involved in CC transfer of GPI to proteins (By similarity). {ECO:0000250}. |
| GO:0042765 GPI-anchor transamidase complex | IBA GO_REF:0000033 | ACCEPT | Summary: Gpi16 is a PIG-T-family GPI-anchor transamidase subunit. Reason: Conserved subunit identity, curated orthology and the target membrane topology support complex membership; the supporting NAS source does not constitute a target purification experiment. Supporting Evidence: file:SCHPO/gpi16/gpi16-uniprot.txt CC -!- FUNCTION: Component of the GPI transamidase complex. Involved in CC transfer of GPI to proteins (By similarity). {ECO:0000250}. PMID:11598210 These complexes can be affinity purified and are shown to consist of Gaa1p, Gpi8p, and Gpi16p (YHR188c). PMID:11483512 PIG-T maintains the complex by stabilizing the expression of GAA1 and GPI8. |
| GO:0042765 GPI-anchor transamidase complex | IEA GO_REF:0000002 | ACCEPT | Summary: Gpi16 is a PIG-T-family GPI-anchor transamidase subunit. Reason: Conserved subunit identity, curated orthology and the target membrane topology support complex membership; the supporting NAS source does not constitute a target purification experiment. Supporting Evidence: file:SCHPO/gpi16/gpi16-uniprot.txt CC -!- FUNCTION: Component of the GPI transamidase complex. Involved in CC transfer of GPI to proteins (By similarity). {ECO:0000250}. PMID:11598210 These complexes can be affinity purified and are shown to consist of Gaa1p, Gpi8p, and Gpi16p (YHR188c). PMID:11483512 PIG-T maintains the complex by stabilizing the expression of GAA1 and GPI8. |
| GO:0042765 GPI-anchor transamidase complex | NAS PMID:15003443 A sensitive predictor for potential GPI lipid modification s... | ACCEPT | Summary: Gpi16 is a PIG-T-family GPI-anchor transamidase subunit. Reason: Conserved subunit identity, curated orthology and the target membrane topology support complex membership; the supporting NAS source does not constitute a target purification experiment. Supporting Evidence: file:SCHPO/gpi16/gpi16-uniprot.txt CC -!- FUNCTION: Component of the GPI transamidase complex. Involved in CC transfer of GPI to proteins (By similarity). {ECO:0000250}. PMID:11598210 These complexes can be affinity purified and are shown to consist of Gaa1p, Gpi8p, and Gpi16p (YHR188c). PMID:11483512 PIG-T maintains the complex by stabilizing the expression of GAA1 and GPI8. |
| GO:0098553 lumenal side of endoplasmic reticulum membrane | IC GO_REF:0000111 | ACCEPT | Summary: The major Gpi16 domain faces the ER lumen. Reason: The curated signal peptide, lumenal region and C-terminal transmembrane helix support the lumenal-side inference. Supporting Evidence: file:SCHPO/gpi16/gpi16-uniprot.txt FT TOPO_DOM 23..493 FT /note="Lumenal" FT /evidence="ECO:0000255" |
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